The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained. Studies aimed at correlating structure and function, and experiments aimed at investigating protein folding are conducted. Structural studies for several proteins have been carried out. These HIV-1 protease, cyanovirin-N, GB1 and mutants thereof. In addition, work was also carried out on a number of protein nucleic acid complexes, including those of the wild-type SRY and a sex-reversal mutant of this protein and the transcriptional activator MarA. New media for partially aligning molecules in the magnetic field were developed, characterized and exploited for measuring residual dipolar couplings.